Copper fist DNA-binding domain (IPR001083)

Short name: Cu_fist_DNA-bd_dom

Overlapping homologous superfamilies

Domain relationships



Some fungal transcription factors contain an N-terminal domain, the copper fist, which seems to be involved in copper-dependent DNA-binding [PMID: 8262047, PMID: 8509391]. These proteins activate the transcription of the metallothionein gene in response to copper. Metallothionein maintains copper levels in yeast [PMID: 3052856, PMID: 8262047]. The copper fist domain, which is similar in structure to metallothionein itself, undergoes a large conformational change on copper-binding that allows DNA-binding. The domain contains a conserved array of zinc-binding residues (Cys-X2-Cys-X8-Cys-X-His) and forms a three-stranded antiparallel beta-sheet with two short helical segments that project from one end of the beta-sheet [PMID: 9665167]. Conserved residues form a basic patch that may be important for DNA binding.

GO terms

Biological Process

GO:0006355 regulation of transcription, DNA-templated

Molecular Function

GO:0003677 DNA binding
GO:0003700 DNA-binding transcription factor activity
GO:0005507 copper ion binding

Cellular Component

GO:0005634 nucleus

Contributing signatures

Signatures from InterPro member databases are used to construct an entry.
PROSITE patterns
PROSITE profiles